scholarly journals N-Glycosylation of Asparagine 8 Regulates Surface Expression of Major Histocompatibility Complex Class I Chain-related Protein A (MICA) Alleles Dependent on Threonine 24

2014 ◽  
Vol 289 (29) ◽  
pp. 20078-20091 ◽  
Author(s):  
Maiken Mellergaard ◽  
Sarah Line Skovbakke ◽  
Christine L. Schneider ◽  
Felicia Lauridsen ◽  
Lars Andresen ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Protein A ◽  
Surface Expression ◽  
Class I ◽  
Complex Class ◽  
Related Protein ◽  
Major Histocompatibility ◽  
Histocompatibility Complex

scholarly journals Human Immunodeficiency Virus Nef Induces Rapid Internalization of the T-Cell Coreceptor CD8αβ

2005 ◽  
Vol 79 (17) ◽  
pp. 11422-11433 ◽  
Author(s):  
Veronique Stove ◽  
Inge Van de Walle ◽  
Evelien Naessens ◽  
Elisabeth Coene ◽  
Christophe Stove ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Surface Expression ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Immunodeficiency Virus ◽  
Β Chain

ABSTRACT Human immunodeficiency virus (HIV) Nef is a membrane-associated protein decreasing surface expression of CD4, CD28, and major histocompatibility complex class I on infected cells. We report that Nef strongly down-modulates surface expression of the β-chain of the CD8αβ receptor by accelerated endocytosis, while CD8 α-chain expression is less affected. By mutational analysis of the cytoplasmic tail of the CD8 β-chain, an FMK amino acid motif was shown to be critical for Nef-induced endocytosis. Although independent of CD4, endocytosis of the CD8 β-chain was abrogated by the same mutations in Nef that affect CD4 down-regulation, suggesting common molecular interactions. The ability to down-regulate the human CD8 β-chain was conserved in HIV-1, HIV-2, and simian immunodeficiency virus SIVmac239 Nef and required an intact AP-2 complex. The Nef-mediated internalization of receptors, such as CD4, major histocompatibility complex class I, CD28, and CD8αβ, may contribute to the subversion of the host immune system and progression towards AIDS.

scholarly journals Transcription of Preintegrated HIV-1 cDNA Modulates Cell Surface Expression of Major Histocompatibility Complex Class I via Nef

2011 ◽  
Vol 85 (6) ◽  
pp. 2828-2836 ◽  
Author(s):  
R. D. Sloan ◽  
B. D. Kuhl ◽  
D. A. Donahue ◽  
A. Roland ◽  
T. Bar-Magen ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Surface Expression ◽  
Class I ◽  
Cell Surface Expression ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Hiv 1

Rat Cytomegalovirus Induces a Temporal Downregulation of Major Histocompatibility Complex Class I Cell Surface Expression

2005 ◽  
Vol 18 (4) ◽  
pp. 607-615 ◽  
Author(s):  
Gerco C. Hassink ◽  
Joanne G. Duijvestijn-Van Dam ◽  
Danijela Koppers-Lalic ◽  
Jacqueline Van Gaans-Van Den Brink ◽  
Daphne Van Leeuwen ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Surface Expression ◽  
Class I ◽  
Cell Surface Expression ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Histocompatibility Complex

scholarly journals Availability of endogenous peptides limits expression of an M3a-Ld major histocompatibility complex class I chimera.

1994 ◽  
Vol 179 (1) ◽  
pp. 155-165 ◽  
Author(s):  
J M Vyas ◽  
R R Rich ◽  
D D Howell ◽  
S M Shawar ◽  
J R Rodgers
Keyword(s):  
Major Histocompatibility Complex ◽  
Cell Surface ◽  
Major Histocompatibility Complex Class ◽  
Surface Expression ◽  
Class I ◽  
Dependent Manner ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Endogenous Peptides ◽  
Histocompatibility Complex

Taking advantage of our understanding of the peptide specificity of the major histocompatibility complex class I-b molecule M3a, we sought to determine why these molecules are poorly represented on the cell surface. To this end we constructed a chimeric molecule with the alpha 1 and alpha 2 domains of M3a and alpha 3 of Ld thereby allowing use of available monoclonal antibodies to quantify surface expression. Transfected, but not control, B10.CAS2 (H-2M3b) cells were lysed readily by M3a-restricted monoclonal cytotoxic T lymphocytes. Thus, the chimera bound, trafficked, and presented endogenous mitochondrial peptides. However, despite high levels of M3a-Ld mRNA, transfectants were negative by surface staining. This finding was consistent with inefficient trafficking to the cell surface. Incubation at 26 degrees C, thought to permit trafficking of unoccupied heavy (H) chains, resulted in detectable cell surface expression of chimeric molecules. Incubation with exogenous peptide at 26 degrees C (but not at 37 degrees C) greatly enhanced expression of M3a-Ld molecules in a dose-dependent manner, suggesting stabilization of unoccupied molecules. Stable association of beta 2-microglobulin with the chimeric H chain was observed in labeled cell lysates only in the presence of exogenous specific peptide, indicating that peptide is required for the formation of a ternary complex. These results indicate that surface expression of M3a-Ld is limited largely by the steady-state availability of endogenous peptides. Since most known M3a-binding peptides are N-formylated, native M3a may normally be expressed at high levels only during infection by intracellular bacteria.

Major Histocompatibility Complex Class I-related Chains A and B (MIC A/B): A Role in the Pathogenesis of Non-alcoholic Steatohepatitis

2009 ◽  
Vol 47 (01) ◽  
Author(s):  
A Kahraman ◽  
S Menziletoglu Yildiz ◽  
M Schlattjan ◽  
A Kilicarslan ◽  
CD Fingas ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Major Histocompatibility Complex Class ◽  
Class I ◽  
Complex Class ◽  
Major Histocompatibility ◽  
Alcoholic Steatohepatitis ◽  
Histocompatibility Complex
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